NMR paper NMR relaxation and water self-diffusion studies in whey protein solutions and gels.

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[NMR paper] NMR relaxation and water self-diffusion studies in whey protein solutions and gels.

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NMR processing:

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NMR assignment:

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Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

I-TASSER

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Amber

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Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

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Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

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RCI

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HADDOCK

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SAVES2 or SAVES4

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Methyl S2

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12-01-2010, 06:56 PM

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NMR relaxation and water self-diffusion studies in whey protein solutions and gels.

NMR relaxation and water self-diffusion studies in whey protein solutions and gels.

Related Articles NMR relaxation and water self-diffusion studies in whey protein solutions and gels.

J Agric Food Chem. 2005 Aug 24;53(17):6784-90

Authors: Colsenet R, Mariette F, Cambert M

The changes in water proton transverse relaxation behavior induced by aggregation of whey proteins are explained in terms of the simple molecular processes of diffusion and chemical exchange. The water self-diffusion coefficient was measured in whey protein solutions and gels by the pulsed field gradient NMR method. As expected, water self-diffusion was reduced with increased protein concentrations. Whatever the concentration, the water molecules were free to diffuse over distances varying from 15 to 47 mum. Water diffusion was constant over these distances, demonstrating that no restrictions were found to explain the water hindrance. The modification in protein structure by gelation induced a decrease in water diffusion. The effects of protein concentration on water diffusion are discussed and modeled. Two approaches were compared, the obstruction effect induced by a spherical particle and the cell model, which considered two water compartments with specific self-diffusion coefficients.

PMID: 16104800 [PubMed - indexed for MEDLINE]

Source: PubMed

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